Hostname: page-component-cd9895bd7-q99xh Total loading time: 0 Render date: 2024-12-29T10:58:29.406Z Has data issue: false hasContentIssue false

Block Copolymer-Based Biomembranes Functionalized with Energy Transduction Proteins

Published online by Cambridge University Press:  17 March 2011

Dean Ho
Affiliation:
Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095, U.S.A
Benjamin Chu
Affiliation:
Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095, U.S.A
Hyeseung Lee
Affiliation:
Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095, U.S.A
Karen Kuo
Affiliation:
Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095, U.S.A
Carlo D. Montemagno
Affiliation:
Department of Bioengineering, University of California, Los Angeles Los Angeles, CA 90095, U.S.A
Get access

Abstract

Block copolymer-based membranes can be functionalized with energy transducing proteins to reveal a versatile family of nanoscale materials. Our work has demonstrated the fabrication of protein-functionalized ABA triblock copolymer nanovesicles that possess a broad applicability towards areas like biosensing and energy production. ABA triblock copolymers possess certain advantages over lipid systems. For example, they can mimic biomembrane environments necessary for membrane protein refolding in a single chain (hydrophilic(A)- hydrophobic(B)-hydrophilic(A)), enabling large-area membrane fabrication using methods like Langmuir-Blodgett (LB) deposition. Furthermore, the robustness of the polymer molecules/structure result in spontaneous and rapid protein-functionalized nano-vesicle formation that retains structure as well as protein functionality for up to several months, compared to one to two weeks for the lipid systems (e.g. POPC). The membrane protein, Bacteriorhodopsin (BR), found in Halobacterium Halobium, is a light-actuated proton pump that develops gradients towards the demonstration of coupled functionality with other membrane proteins, such as the production of electricity through Bacteriorhodopsin activity-dependent reversal of Cytochrome C Oxidase (COX), found in Rhodobacter Sphaeroides. Protein-functionalized materials have the exciting potential of serving as the core technology behind a series of fieldable devices that are driven completely by biomolecules.

Type
Research Article
Copyright
Copyright © Materials Research Society 2004

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Spudich, J. L., Bogolmolni, R.A., “The mechanism of color discrimination by a bacterial sensory,” Nature vol. 312, 509513, (1984).CrossRefGoogle ScholarPubMed
2. Spudich, J.L. Bogolmolni, R.A., “Sensory rhodopsin in halobacteria,” Annu. Rev. Biophys. Chem., vol.17, 193215, (1984).CrossRefGoogle Scholar
3. Steinberg, G., Friedman, N., Sheves, M., Ottolenghi, M., “Isomer composition, and spectra at the dark and light adapted forms at artificial bacteriorhodopsin,” Photochem. Photobiol., vol.54, 969976, (1991).CrossRefGoogle Scholar
4. Stoeckenius, W., “From membrane structure to bacteriorhodopsin,” J. Membr. Biol, vol.. 139, 139148, (1994).CrossRefGoogle ScholarPubMed
5. Meier, W., Nardin, C., Winterhalter, M., “Reconstitution of Channel Proteins in (Polymerized) ABA Triblock Copolymer Membranes,” Angew. Chem. Int. Ed., vol. 39, pp 45994602, (1999).3.0.CO;2-Y>CrossRefGoogle Scholar
6. Winterhalter, M., Hilty, C., Bezrukov, S.M., Nardin, C., Meier, W., Fournier, D., “Controlling Membrane Permeability with Bacterial Porins: Application to Encapsulated Enzymes.” Talanta 55:965971, (2001).CrossRefGoogle ScholarPubMed
7. Nardin, C., Widmer, J. Winterhalter, M., Meier, W., “Amphiphilic Block Copolymer Nanocontainers as Bioreactors.” Eur. Phys. Journ. E. 4:403410, (2001).CrossRefGoogle Scholar
8. Zhen, Y., Qian, J., Follmann, K., Hayward, T., Nilsson, T., Dahn, M., Hilmi, Y., Hamer, A.G., Posler, J.P., Ferguson-Miller, S., Protein expression and purification 13, 326336, (1998).CrossRefGoogle Scholar
9. Nardin, C., Winterhalter, M., Meier, W., “Giant Free-Standing ABA Triblock Copolymer Membranes,” Langmuir vol.16, pp 77087712, (2000).CrossRefGoogle Scholar
10. Winterhalter, M., Klotz, K., Benz, R., in Electromanipulation of Cells, edited byZimmerman, U., Neil, G.A.,CRC Press, Boca Raton, p.137,(1995).Google Scholar
11. Ho, D., Chu, B., Schmidt, J., Brooks, E., Montemagno, C.D., “Hybrid Protein/Polymer Biomimetic Membranes” accepted to IEEE Trans. Nanotechnology June, (2004).CrossRefGoogle Scholar
12. Lee, H., Ho, D., Schmidt, J., Montemagno, C.D., “Reconstitution of energy converting proteins in biocompatible materials,” IEEE Proc. Nanotechnology, vol. 2, 733736, (2003).Google Scholar
13. Hazard, A., Montemagno, C.D., “Improved puri.cation for thermophilic F1F0 ATP synthase using n-dodecyl b-D-maltoside,” Arch. Biochem. Biophys., vol. 407, 117124, (2002).CrossRefGoogle Scholar
14. Gau, J., Lan, E., Dunn, B.. Ho, C.M., Woo, J.,”A MEMS based amperometric detector for E. coli bacteria using self-assembled monolayers,” Biosens. Bioelec., vol. 16, pp. 745755, (2001).CrossRefGoogle ScholarPubMed